This product is monospecific antiserum processed by delipidation and defibrination followed by sterile filtration. This antibody reacts with human and mouse APC11. Cross reactivity may also occur with APC11 from other sources. Sufficient sequence differences exist to suggest that this antibody would not react with other RING box proteins such as ROC1 and ROC2.

Purification

Delipidation and defibrination.

Target details

Target details

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Alternative Name

APC11 / ANAPC11

Background

APC11 is also known as Anaphase promoting complex subunit 11, APC11, Cyclosome subunit 11, Hepatocellular carcinoma associated RING finger protein, and HSPC214. APC11 is a component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. APC11 may function to recruit the E2 ubiquitin-conjugating enzymes to the complex. APC11 interacts with the cullin domain of ANAPC2 and also interacts with UBE2D2. APC11 shows both a cytoplasmic and nuclear localization. APC11 is expressed at high levels in skeletal muscle and heart, in moderate levels in brain, kidney, and liver, and at low levels in colon, thymus, spleen, small intestine, placenta, lung and peripheral blood leukocyte. APC11 is a member of the RING-type zinc finger family and is auto-ubiquitinylated.Synonyms: Anaphase-promoting complex subunit 11, Cyclosome subunit 11, HSPC214, Hepatocellular carcinoma-associated RING finger protein

Application Details

Application Details

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Application Notes

Western blot (1: 500-1: 1,000). ELISA (1: 2,000-1: 10,000). Immunoprecipitation: The antibody immunoprecipitates in vitro translated protein andprotein from overexpressing cell lysates (using HeLa and NIH-3T3, and others). Coimmunoprecipitation of related proteins (APC2) does occur. A 9.8 kDa bandcorresponding to human APC11 is detected. Most cell lines or tissues expressing APC11 canbe used as a positive control. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.

Images

Images

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Supplier Images

Conjugation pathways for ubiquitin and ubiquitin-like modifiers (UBLs). Most modifiers mature by proteolytic processing from inactive precursors (a, amino acid). Arrowheads point to the cleavage sites. Ubiquitin is expressed either as polyubiquitin or as a fusion with ribosomal proteins. Conjugation requires activating (E1) and conjugating (E2) enzymes that form thiolesters (S) with the modifiers. Modification of cullins by RUB involves SCF(SKP1/cullin-1/F-box protein) /CBC(cullin-2/elongin B/elonginC) -like E3 enzymes that are also involved in ubiquitination. In contrast to ubiquitin, the UBLs do not seem to form multi-UBL chains. UCRP(ISG15) resembles two ubiquitin moieties linked headto- tail. Whether HUB1 functions as a modifier is currently unclear. APG12 and URM1 are distinct from the other modifiers because they are unrelated in sequence to ubiquitin. Data contributed by S.Jentsch, see references below.

Conjugation pathways for ubiquitin and ubiquitin-like modifiers (UBLs). Most modifiers mature by proteolytic processing from inactive precursors (a, amino acid). Arrowheads point to the cleavage sites. Ubiquitin is expressed either as polyubiquitin or as a fusion with ribosomal proteins. Conjugation requires activating (E1) and conjugating (E2) enzymes that form thiolesters (S) with the modifiers. Modification of cullins by RUB involves SCF(SKP1/cullin-1/F-box protein) /CBC(cullin-2/elongin B/elonginC) -like E3 enzymes that are also involved in ubiquitination. In contrast to ubiquitin, the UBLs do not seem to form multi-UBL chains. UCRP(ISG15) resembles two ubiquitin moieties linked headto- tail. Whether HUB1 functions as a modifier is currently unclear. APG12 and URM1 are distinct from the other modifiers because they are unrelated in sequence to ubiquitin. Data contributed by S.Jentsch, see references below.

Gmachl, Gieffers, Podtelejnikov et al.: "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, Issue 16, pp. 8973-8, 2000 (PubMed).

Jentsch, Pyrowolakis: "Ubiquitin and its kin: how close are the family ties?" in: Trends in cell biology, Vol. 10, Issue 8, pp. 335-42, 2000 (PubMed).